Experiments were made on male killifish, Fundulus heteroclitus, weighing ca. 10 g, to determine whether the melanophore dispersing hormones, α - or β-MSH, could enter the general circulation after injection into the third brain ventricle. Each fish had an implanted cannula provided with a removable cap for intracranial injection. The presence of a dispersing hormone in the blood was detected by means of the darkening of a “faded denervated caudal band,” described by Parker (1948). After injection, unanesthetized fish were observed for 60 min against a white background. Intraperitoneal injections of .67 µg, or less, of either preparation, in 100 µl of.6% NaCl, elicited the expected darkening with a latency of 10.7±.9 (SEM) min; intracranial injections of the same dose in .3 µl had no effect (seven fish) or resulted in a scarcely detectable darkening with a long-delayed latency (three fish). The melanophore hormones, α- and β-MSH pass the CSF-blood barrier with difficulty, if at all.
The naturally occurring corticosteroids, cortisol and aldosterone, failed to promote survival of hypophysectomized Fundulus heteroclitus in fresh water. Extracts of Fundulus interrenal tissue, carp corpuscles of Stannius, and hog renin were ineffective. Injection of whole rat-pituitary brei was partially successful. Highly purified prolactin maintained survival, although the recipients did not eat normally. A synergic action of prolactin with some unidentified pituitary hormone is suspected.
Journal Article FURTHER STUDIES OF THE HORMONAL INDUCTION OF MELANOGENESIS IN THE KILLIFISH, FUNDULUS HETEROCLITUS Get access BERNARD KOSTO, BERNARD KOSTO 1Bingham Oceanographic Laboratory, Yale University and Section of Dermatology, Yale University School of Medicine New Haven, Connecticut Search for other works by this author on: Oxford Academic Google Scholar GRACE E. PICKFORD, GRACE E. PICKFORD 1Bingham Oceanographic Laboratory, Yale University and Section of Dermatology, Yale University School of Medicine New Haven, Connecticut Search for other works by this author on: Oxford Academic Google Scholar MORRIS FOSTER MORRIS FOSTER 1Bingham Oceanographic Laboratory, Yale University and Section of Dermatology, Yale University School of Medicine New Haven, Connecticut Search for other works by this author on: Oxford Academic Google Scholar Endocrinology, Volume 65, Issue 6, 1 December 1959, Pages 869–881, https://doi.org/10.1210/endo-65-6-869 Published: 01 December 1959 Article history Received: 11 May 1959 Published: 01 December 1959
Fish farming could be much more important than it is, particularly in areas of overpopulation and malnutrition. The problem has always been that many food-fish will not spawn in captivity. One possible solution lies in the use of pituitary extracts, which stimulate spawning. These have been found of value both for intensive fish cultivation and for solving the problems caused by damming the rivers in the Soviet Union in which the sturgeon breed. The experiments, results, and some applications are described in this article.
THE experiments reported in this investigation were instigated by the accidental discovery, described below (Series XXI), that chronic treatment with prolactin stimulated melanogenesis in hypophysectomized killifish, Fundulus heteroclitus (Linn.). In discussing the complex problems involved, a distinction must be made between 1) physiological regulation of the state of concentration or dispersion of the melanophores, and 2) morphological processes of depigmentation, melanization, and new pigment cell formation. It has been repeatedly pointed out that the two phenomena appear to be interrelated (1, 2). Conditions which favor melanophore dispersion (illumination against a dark background, blinding) promote increased pigmentation and the development of new pigment cells. Conditions which favor aggregation of the melanin granules (illumination against a light background) retard or inhibit the development of melanophores and lead to a partial loss of pigment from cells already present. This is to be expected since the afferent pathways, through the photoreceptors, are the same.
Previous investigations (Pickford, 1953b; 1954) have shown that highly purified beef growth hormone preparations contained sufficient thyrotropin to maintain the thyroids of hypophysectomized killifish at a normal level of activity, although there was no evidence of hyper-stimulation. According to Dr. A. E. Wilhelmi, who supplied the growth hormone preparations, the presence of thyrotropin could not be detected by the rat test and it was believed that a contamination of the order of 1% was the maximum that could be expected. The following experiment was undertaken at his suggestion to determine the minimum amount of a standard preparation of thyrotropin that would be sufficient to account for the results noted above. Since the growth hormone was administered at a dosage level of 10 mg. per gram weight thrice weekly, the treatment with thyrotropin was calculated to straddle the 1% level of contamination, at 1 mg. 0.1 mg. and 0.01 mg. per gm. weight.
Journal Article A NOTE ON THE EGGS OF OCTOPUS VULGARIS LAM. FROM THE WESTERN ATLANTIC : THE IDENTITY OF TANDY'S EGGS FROM THE DRY TORTUGAS Get access GRACE E. PICKFORD GRACE E. PICKFORD Bingham Oceanographic Laboratory, Yale University Search for other works by this author on: Oxford Academic Google Scholar Journal of Molluscan Studies, Volume 28, Issue 2-3, 24 March 1950, Pages 88–92, https://doi.org/10.1093/oxfordjournals.mollus.a064572 Published: 24 March 1950 Article history Received: 13 May 1949 Published: 24 March 1950
THE OCTOPODA OF THE OXFORD UNIVERSITY CAYMAN EXPEDITION Get access GRACE E. PICKFORD, PH.D. GRACE E. PICKFORD, PH.D. Bingham Oceanographic Laboratory, Yale University Search for other works by this author on: Oxford Academic Google Scholar Journal of Molluscan Studies, Volume 28, Issue 4-5, 18 December 1950, Pages 139–144, https://doi.org/10.1093/oxfordjournals.mollus.a064576 Published: 18 December 1950 Article history Received: 10 June 1949 Published: 18 December 1950
Journal of Experimental ZoologyVolume 92, Issue 2 p. 143-170 Article The distribution of dipeptidase in the salamander gastrula Grace E. Pickford, Grace E. Pickford Osborn Zoological Laboratory, Yale University, New Haven, ConnecticutSearch for more papers by this author Grace E. Pickford, Grace E. Pickford Osborn Zoological Laboratory, Yale University, New Haven, ConnecticutSearch for more papers by this author First published: March 1943 https://doi.org/10.1002/jez.1400920203Citations: 6AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat Literature Cited Avery, G. S., and K. Linderstrøm-Lang 1940 Peptidase activity in the Avena coleoptile, phytohormone test object. Bot. Gaz., vol., 102, pp. 50–63. Boell, E. J., J. Needham and V. Rogers 1939 Morphogenesis and metabolism: studies with the Cartesian diver ultramicromanometer. I. Anaerobic glycolysis of the regions of the amphibian gastrula. Proc. R. Soc. London, ser. B, vol. 127, pp. 322–356. Boell, E. J., J. Needham and V. Rogers 1939 Morphogenesis and metabolism: studies with the Cartesian diver ultramicromanometer. II. Effect of dinitro-o-cresol on the anaerobic glycolysis of the regions of the amphibian gastrula. Proc. R. Soc. London, ser. B, vol. 127, pp. 356–362. Boell, E. J., H. Koch and J. Needham 1939 Morphogenesis and metabolism: studies with the Cartesian diver ultramicromanometer. III. Respiratory rate of the regions of the amphibian gastrula. Proc. R. Soc. London, ser. B, vol. 127, pp. 363–373. Boell, E. J., H. Koch and J. Needham 1939 Morphogenesis and metabolism: studies with the Cartesian diver ultramicromanometer. IV. Respiratory quotient of the regions of the amphibian gastrula. Proc. R. Soc. London, ser. B, vol. 127, pp. 374–387. Dole, M. 1941 The Glass Electrode. John Wiley and Sons, New York. Povle, W. L. 1938 Studies on enzymatic histochemistry. XXVII. Peptidase and catalase activity of marine ova. C. R. Lab. Carlsberg, ser. chim., vol. 21, pp. 291–300. Duspiva, F. 1936 Beitrage zur enzymatischen Histochimie. XXI. Die proteolytischen Enzyme der Kleider- und Wachsmottenraupen. C. R. Lab. Carlsberg, ser. chim., vol. 21, pp. 177–202. Holter, H. 1936 Studies on enzymatic histochemistry. XVIII. Localization of peptidase in marine ova. J. Cell. and Comp. Physiol., vol. 8, pp. 179–199. Holter, H. 1939 Arch. Exp. Zelforsch. Gewebezucht, vol. 22, p. 534. (Original not seen, abstract courtesy of Dr. E. J. Boell.) Holter, H., and W. L. Doyle 1937 Uber die Lokalisation der Amylase in Amoben. C. R. Lab. Carlsberg, ser. chim., vol. 22, pp. 219–225. Holter, H., 1938 Studies on enzymatic histochemistry. XXVIII. Enzymatic studies on Protozoa. J. Cell. and Comp. Physiol., vol. 12, pp. 295–308. Holter, H., and M. J. Kopac 1937 Studies on enzymatic histochemistry. XXIV. Localization of peptidase in Ameba. J. Cell. and Comp. Physiol., vol. 10, pp. 423–437. Holter, H., H. Lanz and K. Linderstrøm-Lang 1938 Beitrage zur enzymatischen Histochimie. XXX. Lokalisierung der Peptidase wahrend der ersten Furchungen des Eies von Psammechinus miliaris. C. R. Lab. Carlsberg, ser. chim., vol. 23, pp. 1–10. Levy, M. 1936 Studies on enzymatic histochemistry. XVII. A micro Kjeldahl estimation. C. R. Lab. Carlsberg, vol. 21, pp. 101–110. Levy, M., and A. H. Palmer 1940 Chemistry of the chick embryo. II. Weight, nitrogen and dipeptidase accumulation. J. Biol. Chem., vol. 136, pp. 415–423. Linderstrøm-Lang, K. 1933 Studies on enzymatic histochemistry. IV. The peptidase content of some marine invertebrates. C. R. Lab. Carlsberg, ser. chim., vol. 19, part 13, pp. 1–13. Linderstrøm-Lang, K., and H. Holter 1931 Contribution to the histological chemistry of enzymes. I. The estimation of small cleavages caused by enzymes. C. R. Lab. Carlsberg, ser. chim., vol. 19, part 4, pp. 1–19. Linderstrøm-Lang, K., and H. Holter 1932 Contribution to the histological chemistry of enzymes. II. The distribution of peptidase in the roots and sprouts of malt. C. R. Lab. Carlsberg, ser. chim., vol. 19, part 6, pp. 1–39. Linderstrøm-Lang, K., and H. Holter 1933 Studies on enzymatic histochemistry. V. A micro-method for the estimation of sugars. C. R. Lab. Carlsberg, ser. chim., vol. 19, part 14, pp. 1–12. Linderstrøm-Lang, K., and H. Holter 1935 Studies on enzymatic histochemistry. XI. The distribution of peptidase in the gastric and duodenal mucosa of the pig. C. R. Lab. Carlsberg, ser. chim., vol. 20, part 11, pp. 42–56. Linderstrøm-Lang, K., and H. Holter 1940 Verteilung einiger Enzyme in den Schleimhaut-schichten des Magendarmkanales einiger Vertebraten. C. R. Lab. Carlsberg, ser. chim., vol. 23, pp. 135–148. Palmer, A. H., and M. Levy 1940a Chemistry of the chick embryo. I. The dipeptidase of chick embryo extracts. J. Biol. Chem., vol. 136, pp. 407–413. Palmer, A. H., and M. Levy 1940b Chemistry of the chick embryo. III. Distribution of dipeptidase in the cephalic region of the three day embryo. J. Biol. Chem., vol. 136, pp. 629–635. Philipson, T. 1934 Studies on enzymatic histochemistry. VII. The peptidase in the eggs of Psammechinus miliaris. C. R. Lab. Carlsberg. vol. 20, part 4, pp. 1–8. Pickford, G. E. 1937 A sealed-in micro glass electrode. Proc. Soc. Exp. Biol. Med., vol. 36, pp. 154–157. Strain, H. H. 1940 Extraction of proteins and proteolytic enzymes from yeast. C. R. Lab. Carlsberg, ser. chim., vol. 23, pp. 149–162. Citing Literature Volume92, Issue2March 1943Pages 143-170 ReferencesRelatedInformation